pyridoxal 5'-phosphate synthase glutaminase subunit PdxT [Micrococcus porci]
PdxT family protein( domain architecture ID 10785267)
PdxT family protein
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
PdxT | COG0311 | Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) [Coenzyme transport ... |
6-212 | 4.15e-84 | ||||
Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) [Coenzyme transport and metabolism]; Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis : Pssm-ID: 440080 [Multi-domain] Cd Length: 191 Bit Score: 247.67 E-value: 4.15e-84
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Name | Accession | Description | Interval | E-value | ||||
PdxT | COG0311 | Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) [Coenzyme transport ... |
6-212 | 4.15e-84 | ||||
Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) [Coenzyme transport and metabolism]; Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis Pssm-ID: 440080 [Multi-domain] Cd Length: 191 Bit Score: 247.67 E-value: 4.15e-84
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PRK13525 | PRK13525 | pyridoxal 5'-phosphate synthase glutaminase subunit PdxT; |
6-212 | 1.44e-83 | ||||
pyridoxal 5'-phosphate synthase glutaminase subunit PdxT; Pssm-ID: 237411 [Multi-domain] Cd Length: 189 Bit Score: 246.22 E-value: 1.44e-83
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GATase1_PB | cd01749 | Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine ... |
8-212 | 3.22e-80 | ||||
Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis. Glutamine amidotransferase (GATase) activity involves the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. This group contains proteins like Bacillus subtilus YaaE and Plasmodium falciparum Pdx2 which are members of the triad glutamine aminotransferase family and function in a pathway for the biosynthesis of vitamin B6. Pssm-ID: 153220 [Multi-domain] Cd Length: 183 Bit Score: 237.42 E-value: 3.22e-80
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PLP_synth_Pdx2 | TIGR03800 | pyridoxal 5'-phosphate synthase, glutaminase subunit Pdx2; Pyridoxal 5'-phosphate (PLP) is ... |
8-213 | 2.18e-63 | ||||
pyridoxal 5'-phosphate synthase, glutaminase subunit Pdx2; Pyridoxal 5'-phosphate (PLP) is synthesized by the PdxA/PdxJ pathway in some species (mostly within the gamma subdivision of the proteobacteria) and by the Pdx1/Pdx2 pathway in most other organisms. This family describes Pdx2, the glutaminase subunit of the PLP synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine] Pssm-ID: 274792 [Multi-domain] Cd Length: 184 Bit Score: 194.96 E-value: 2.18e-63
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SNO | pfam01174 | SNO glutamine amidotransferase family; This family and its amidotransferase domain was first ... |
10-212 | 1.71e-43 | ||||
SNO glutamine amidotransferase family; This family and its amidotransferase domain was first described in. It is predicted that members of this family are involved in the pyridoxine biosynthetic pathway, based on the proximity and co-regulation of the corresponding genes and physical interaction between the members of pfam01174 and pfam01680. Pssm-ID: 334414 [Multi-domain] Cd Length: 188 Bit Score: 144.21 E-value: 1.71e-43
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Name | Accession | Description | Interval | E-value | ||||
PdxT | COG0311 | Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) [Coenzyme transport ... |
6-212 | 4.15e-84 | ||||
Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) [Coenzyme transport and metabolism]; Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis Pssm-ID: 440080 [Multi-domain] Cd Length: 191 Bit Score: 247.67 E-value: 4.15e-84
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PRK13525 | PRK13525 | pyridoxal 5'-phosphate synthase glutaminase subunit PdxT; |
6-212 | 1.44e-83 | ||||
pyridoxal 5'-phosphate synthase glutaminase subunit PdxT; Pssm-ID: 237411 [Multi-domain] Cd Length: 189 Bit Score: 246.22 E-value: 1.44e-83
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GATase1_PB | cd01749 | Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine ... |
8-212 | 3.22e-80 | ||||
Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis. Glutamine amidotransferase (GATase) activity involves the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. This group contains proteins like Bacillus subtilus YaaE and Plasmodium falciparum Pdx2 which are members of the triad glutamine aminotransferase family and function in a pathway for the biosynthesis of vitamin B6. Pssm-ID: 153220 [Multi-domain] Cd Length: 183 Bit Score: 237.42 E-value: 3.22e-80
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PLP_synth_Pdx2 | TIGR03800 | pyridoxal 5'-phosphate synthase, glutaminase subunit Pdx2; Pyridoxal 5'-phosphate (PLP) is ... |
8-213 | 2.18e-63 | ||||
pyridoxal 5'-phosphate synthase, glutaminase subunit Pdx2; Pyridoxal 5'-phosphate (PLP) is synthesized by the PdxA/PdxJ pathway in some species (mostly within the gamma subdivision of the proteobacteria) and by the Pdx1/Pdx2 pathway in most other organisms. This family describes Pdx2, the glutaminase subunit of the PLP synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine] Pssm-ID: 274792 [Multi-domain] Cd Length: 184 Bit Score: 194.96 E-value: 2.18e-63
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PRK13527 | PRK13527 | glutamine amidotransferase subunit PdxT; Provisional |
7-212 | 1.83e-59 | ||||
glutamine amidotransferase subunit PdxT; Provisional Pssm-ID: 237412 [Multi-domain] Cd Length: 200 Bit Score: 185.48 E-value: 1.83e-59
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PLN02832 | PLN02832 | glutamine amidotransferase subunit of pyridoxal 5'-phosphate synthase complex |
7-212 | 1.12e-51 | ||||
glutamine amidotransferase subunit of pyridoxal 5'-phosphate synthase complex Pssm-ID: 215446 [Multi-domain] Cd Length: 248 Bit Score: 167.19 E-value: 1.12e-51
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SNO | pfam01174 | SNO glutamine amidotransferase family; This family and its amidotransferase domain was first ... |
10-212 | 1.71e-43 | ||||
SNO glutamine amidotransferase family; This family and its amidotransferase domain was first described in. It is predicted that members of this family are involved in the pyridoxine biosynthetic pathway, based on the proximity and co-regulation of the corresponding genes and physical interaction between the members of pfam01174 and pfam01680. Pssm-ID: 334414 [Multi-domain] Cd Length: 188 Bit Score: 144.21 E-value: 1.71e-43
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PRK13526 | PRK13526 | glutamine amidotransferase subunit PdxT; Provisional |
7-213 | 5.88e-31 | ||||
glutamine amidotransferase subunit PdxT; Provisional Pssm-ID: 184113 [Multi-domain] Cd Length: 179 Bit Score: 111.97 E-value: 5.88e-31
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hisH | PRK13181 | imidazole glycerol phosphate synthase subunit HisH; Provisional |
15-112 | 1.32e-12 | ||||
imidazole glycerol phosphate synthase subunit HisH; Provisional Pssm-ID: 183878 [Multi-domain] Cd Length: 199 Bit Score: 63.73 E-value: 1.32e-12
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GATase1_CobQ | cd01750 | Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type ... |
21-114 | 1.38e-08 | ||||
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ). CobQ plays a role in cobalamin biosythesis. CobQ catalyses amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide in the biosynthesis of cobalamin. CobQ belongs to the triad family of amidotransferases. Two of the three residues of the catalytic triad that are involved in glutamine binding, hydrolysis and transfer of the resulting ammonia to the acceptor substrate in other triad aminodotransferases are conserved in CobQ. Pssm-ID: 153221 [Multi-domain] Cd Length: 194 Bit Score: 52.63 E-value: 1.38e-08
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hisH | PRK13143 | imidazole glycerol phosphate synthase subunit HisH; Provisional |
24-112 | 1.84e-08 | ||||
imidazole glycerol phosphate synthase subunit HisH; Provisional Pssm-ID: 237289 [Multi-domain] Cd Length: 200 Bit Score: 52.56 E-value: 1.84e-08
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GATase1 | cd01653 | Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
8-97 | 1.59e-07 | ||||
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Pssm-ID: 153210 [Multi-domain] Cd Length: 115 Bit Score: 48.36 E-value: 1.59e-07
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GATase1_CobB | cd03130 | Type 1 glutamine amidotransferase (GATase1) domain found in Cobyrinic Acid a,c-Diamide ... |
18-111 | 4.12e-07 | ||||
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyrinic Acid a,c-Diamide Synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Cobyrinic Acid a,c-Diamide Synthase. CobB plays a role in cobalamin biosythesis catalyzing the conversion of cobyrinic acid to cobyrinic acid a,c-diamide. CobB belongs to the triad family of amidotransferases. Two of the three residues of the catalytic triad that are involved in glutamine binding, hydrolysis and transfer of the resulting ammonia to the acceptor substrate in other triad aminodotransferases are conserved in CobB. Pssm-ID: 153224 [Multi-domain] Cd Length: 198 Bit Score: 48.36 E-value: 4.12e-07
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GATase_3 | pfam07685 | CobB/CobQ-like glutamine amidotransferase domain; |
44-111 | 5.59e-07 | ||||
CobB/CobQ-like glutamine amidotransferase domain; Pssm-ID: 429595 [Multi-domain] Cd Length: 189 Bit Score: 48.01 E-value: 5.59e-07
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GAT_1 | cd03128 | Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
15-89 | 2.02e-06 | ||||
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain. Pssm-ID: 153222 [Multi-domain] Cd Length: 92 Bit Score: 44.50 E-value: 2.02e-06
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CobB | COG1797 | Cobyrinic acid a,c-diamide synthase [Coenzyme transport and metabolism]; Cobyrinic acid a, ... |
18-116 | 2.75e-06 | ||||
Cobyrinic acid a,c-diamide synthase [Coenzyme transport and metabolism]; Cobyrinic acid a,c-diamide synthase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis Pssm-ID: 441402 [Multi-domain] Cd Length: 459 Bit Score: 47.03 E-value: 2.75e-06
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PRK01077 | PRK01077 | cobyrinate a,c-diamide synthase; |
19-116 | 1.03e-05 | ||||
cobyrinate a,c-diamide synthase; Pssm-ID: 234896 [Multi-domain] Cd Length: 451 Bit Score: 45.51 E-value: 1.03e-05
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hisH | CHL00188 | imidazole glycerol phosphate synthase subunit hisH; Provisional |
34-112 | 6.36e-04 | ||||
imidazole glycerol phosphate synthase subunit hisH; Provisional Pssm-ID: 214389 [Multi-domain] Cd Length: 210 Bit Score: 39.48 E-value: 6.36e-04
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PRK03619 | PRK03619 | phosphoribosylformylglycinamidine synthase subunit PurQ; |
18-92 | 8.74e-04 | ||||
phosphoribosylformylglycinamidine synthase subunit PurQ; Pssm-ID: 235140 [Multi-domain] Cd Length: 219 Bit Score: 38.94 E-value: 8.74e-04
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Blast search parameters | ||||
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